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Literature DB >> 20147749

Chemical approaches for studying histone modifications.

Abstract

Histones form the protein core around which genomic DNA is wrapped in eukaryotic chromatin. Numerous genetic studies have established that the structure and transcriptional state of chromatin are closely related to histone post-translational modifications. Further elucidation of the precise mechanistic roles for individual histone modifications requires the ability to isolate and study homogeneously modified histones. However, the highly heterogeneous nature of histone modifications in vivo poses a significant challenge for such studies. Chemical tools that have enabled biochemical and biophysical studies of site-specifically modified histones are the focus of this minireview.

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Year: 2010 PMID： 20147749 PMCID： PMC2856977 DOI： 10.1074/jbc.R109.080291

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

46 in total

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Journal: Science Date: 2000-05-26 Impact factor: 47.728

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Authors: Michael A Shogren-Knaak; Christopher J Fry; Craig L Peterson
Journal: J Biol Chem Date: 2003-02-20 Impact factor: 5.157

3. Facile synthesis of site-specifically acetylated and methylated histone proteins: reagents for evaluation of the histone code hypothesis.

Authors: Shu He; David Bauman; Jamaine S Davis; Alejandra Loyola; Kenichi Nishioka; Jennifer L Gronlund; Danny Reinberg; Fanyu Meng; Neil Kelleher; Dewey G McCafferty
Journal: Proc Natl Acad Sci U S A Date: 2003-10-06 Impact factor: 11.205

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Journal: Tetrahedron Date: 1967-05 Impact factor: 2.457

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Journal: Nature Date: 1997-09-18 Impact factor: 49.962

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Journal: J Biol Chem Date: 1974-01-10 Impact factor: 5.157

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Authors: J A Butler
Journal: Nature Date: 1965-09-04 Impact factor: 49.962

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10. Structure-activity analysis of semisynthetic nucleosomes: mechanistic insights into the stimulation of Dot1L by ubiquitylated histone H2B.

Authors: Robert K McGinty; Maja Köhn; Champak Chatterjee; Kyle P Chiang; Matthew R Pratt; Tom W Muir
Journal: ACS Chem Biol Date: 2009-11-20 Impact factor: 5.100

37 in total

1. Nucleosome competition reveals processive acetylation by the SAGA HAT module.

Authors: Alison E Ringel; Anne M Cieniewicz; Sean D Taverna; Cynthia Wolberger
Journal: Proc Natl Acad Sci U S A Date: 2015-09-23 Impact factor: 11.205

2. Thiol Specific and Tracelessly Removable Bioconjugation via Michael Addition to 5-Methylene Pyrrolones.

Authors: Yingqian Zhang; Xiaoping Zhou; Yonghui Xie; Marc M Greenberg; Zhen Xi; Chuanzheng Zhou
Journal: J Am Chem Soc Date: 2017-04-20 Impact factor: 15.419

3. Histone monoubiquitylation position determines specificity and direction of enzymatic cross-talk with histone methyltransferases Dot1L and PRC2.

Authors: Sarah J Whitcomb; Beat Fierz; Robert K McGinty; Matthew Holt; Takashi Ito; Tom W Muir; C David Allis
Journal: J Biol Chem Date: 2012-05-22 Impact factor: 5.157

Chemical approaches for studying histone modifications.

1. Structure and function of a human TAFII250 double bromodomain module.

2. A native peptide ligation strategy for deciphering nucleosomal histone modifications.

3. Facile synthesis of site-specifically acetylated and methylated histone proteins: reagents for evaluation of the histone code hypothesis.

4. Mechanistic studies of peptide oxazolone racemization.

5. Crystal structure of the nucleosome core particle at 2.8 A resolution.

6. Chemical studies of histone acetylation. Substrate specificity of a histone deacetylase from calf thymus nuclei.

7. Optical inducation during biomimetic formation of cysteine.

8. Role of histones and other proteins in gene control.

9. Synthesis of proteins by native chemical ligation.

10. Structure-activity analysis of semisynthetic nucleosomes: mechanistic insights into the stimulation of Dot1L by ubiquitylated histone H2B.

1. Nucleosome competition reveals processive acetylation by the SAGA HAT module.

2. Thiol Specific and Tracelessly Removable Bioconjugation via Michael Addition to 5-Methylene Pyrrolones.

3. Histone monoubiquitylation position determines specificity and direction of enzymatic cross-talk with histone methyltransferases Dot1L and PRC2.

4. Scratching the (lateral) surface of chromatin regulation by histone modifications.

5. Chromatin: a ubiquitin crowbar opens chromatin.

Review 6. Combinatorial readout of dual histone modifications by paired chromatin-associated modules.

7. Histone fold modifications control nucleosome unwrapping and disassembly.

Review 8. Pioneer factors and their in vitro identification methods.

9. Preparing semisynthetic and fully synthetic histones h3 and h4 to modify the nucleosome core.

10. Late stage modification of receptors identified from dynamic combinatorial libraries.